10.1021/cb200497q.s001
Yogo Sakakibara
Yogo
Sakakibara
Christine S. Chow
Christine S.
Chow
Role of Pseudouridine
in Structural Rearrangements
of Helix 69 During Bacterial Ribosome Assembly
American Chemical Society
2012
helix 69 dynamics
Bacterial Ribosome AssemblyAs part
role
23 S rRNA
helix 69
70 S ribosomes
protein translation factors
50 S subunits
16 S rRNA
2012-05-18 00:00:00
Journal contribution
https://acs.figshare.com/articles/journal_contribution/Role_of_Pseudouridine_in_Structural_Rearrangements_of_Helix_69_During_Bacterial_Ribosome_Assembly/2521321
As part of the central core domain of the ribosome, helix
69 of
23S rRNA participates in an important intersubunit bridge and contacts
several protein translation factors. Helix 69 is believed to play
key roles in protein synthesis. Even though high-resolution crystal
structures of the ribosome exist, the solution dynamics and roles
of individual nucleotides in H69 are still not well-defined. To better
understand the influence of modified nucleotides, specifically pseudouridine,
on the multiple conformational states of helix 69 in the context of
50S subunits and 70S ribosomes, chemical probing analyses were performed
on wild-type and pseudouridine-deficient bacterial ribosomes. Local
structural rearrangements of helix 69 upon ribosomal subunit association
and interactions with its partner, helix 44 of 16S rRNA, are observed.
The helix 69 conformational states are also magnesium-dependent. The
probing data presented in this study provide insight into the functional
role of helix 69 dynamics and regulation of these conformational states
by post-transcriptional pseudouridine modification.